Effect of Ultrasonic Treatment on Freeze-thaw Stability of Soy Protein Isolate Gel

J Oleo Sci. 2019 Nov 7;68(11):1113-1123. doi: 10.5650/jos.ess19167. Epub 2019 Oct 15.

Abstract

This study investigated the impact of ultrasonic modification at various ultrasonic power extents on the freeze-thaw stability of soy protein isolate (SPI) gel. The freeze-thaw stability of the gel was evaluated by examining the changes in texture, water holding capacity, microstructure and soluble protein content during the process of 5 freeze-thaw cycles. In addition, effects on particle size, surface hydrophobicity and structure were also explored. The results showed that within a certain range, the average particle size of the protein gradually decreased, and the particle size distribution was narrower with ultrasonic intensity, it may be due to the high shear and cavitation effects of sonication that reduce the degree of protein aggregation. Furthermore, we also detected that treated proteins had lower fluorescence intensity, higher surface hydrophobicity and more flexible molecular structure with the reduction of α-helical structure as well as the rise of random coil. In terms of gel freeze-thaw stability, moderate ultrasound treatment made the water holding capacity and soluble protein content of SPI gel reduce by 38.27% and 3.58%, whereas the hardness and elasticity increased by 510.23g and 0.06mm after 5 FTC. The corresponding changes of indexes of the control group were 75.05%, 51%, 1062.75g and 0.11mm, respectively. It can be observed that the change range of treated SPI gel properties was smaller than that of natural SPI gel, indicating that ultrasonic treatment can remarkably improve the freeze-thaw stability of the gel which might have something to do with changes of protein structure.

Keywords: effect; freeze-thaw stability; protein gel; ultrasound treatment.

MeSH terms

  • Elasticity
  • Freezing*
  • Gels
  • Hardness
  • Hydrophobic and Hydrophilic Interactions
  • Molecular Structure
  • Protein Aggregates
  • Protein Stability*
  • Soybean Proteins / chemistry*
  • Ultrasonics*

Substances

  • Gels
  • Protein Aggregates
  • Soybean Proteins